推薦產品
生物源
human
品質等級
重組細胞
expressed in Saccharomyces cerevisiae
形狀
liquid
比活性
≥0.5 units/pmol enzyme
secondary activity
≥100 units/mg protein (Reductase activity)
濃度
≥1 pmol/μL (P450)
≥10 mg/mL protein
UniProt登錄號
運輸包裝
dry ice
儲存溫度
−70°C
基因資訊
human ... CYP1A2(1544)
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一般說明
Microsome contents of CYP1A2 human and yeast CYP-reductase expressed in Saccharomyces cerevisiae.
單位定義
P450 Activity: One unit will oxidize 1 picomole of ethoxyresorufin per minute at pH 7.4 at 28 °C.
Reductase Activity: One unit will reduce 1 nanomole of cytochrome C per minute in the presence of NADPH at pH 7.4 at 28 °C.
Reductase Activity: One unit will reduce 1 nanomole of cytochrome C per minute in the presence of NADPH at pH 7.4 at 28 °C.
外觀
50 mM Tris (pH 7.4), 1 mM EDTA, 20% glycerol
其他說明
For more more information visit our drug metabolism resources for Cytochrome P450 microsome preparations.
儲存類別代碼
12 - Non Combustible Liquids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
分析證明 (COA)
輸入產品批次/批號來搜索 分析證明 (COA)。在產品’s標籤上找到批次和批號，寫有 ‘Lot’或‘Batch’.。
Gowtham Sathyanarayanan et al.
Micromachines, 9(12) (2018-12-14)
This work describes the interfacing of electrowetting-on-dielectric based digital microfluidic (DMF) sample preparation devices with ambient mass spectrometry (MS) via desorption atmospheric pressure photoionization (DAPPI). The DMF droplet manipulation technique was adopted to facilitate drug distribution and metabolism assays in
Haining Zhou et al.
Chemical research in toxicology, 33(7), 1960-1968 (2020-06-03)
Fraxinellone, a furanoid, is one of the bioactive and potentially hepatotoxic constituents from Dictamnus dasycarpus Turcz, which is extensively spread throughout Asian countries. This herb was reported to cause liver injury in clinical application. However, the mechanism behind is still
Miyabi Ito et al.
Drug metabolism and pharmacokinetics, 30(3), 247-252 (2015-05-30)
Genetic variations in cytochrome P450 1A2 (CYP1A2) are associated with interindividual variability in the metabolism and efficacy of many medications. Twenty CYP1A2 variants harboring amino acid substitutions were analyzed for functional changes in enzymatic activity. Recombinant CYP1A2 variant proteins were
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